ID   A9D334_9GAMM            Unreviewed;       582 AA.
AC   A9D334;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=5'-nucleotidase, putative {ECO:0000313|EMBL:EDQ01609.1};
GN   ORFNames=KT99_16119 {ECO:0000313|EMBL:EDQ01609.1};
OS   Shewanella benthica KT99.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=314608 {ECO:0000313|EMBL:EDQ01609.1, ECO:0000313|Proteomes:UP000005839};
RN   [1] {ECO:0000313|EMBL:EDQ01609.1, ECO:0000313|Proteomes:UP000005839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT99 {ECO:0000313|EMBL:EDQ01609.1,
RC   ECO:0000313|Proteomes:UP000005839};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDQ01609.1}.
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DR   EMBL; ABIC01000008; EDQ01609.1; -; Genomic_DNA.
DR   RefSeq; WP_005497725.1; NZ_ABIC01000008.1.
DR   AlphaFoldDB; A9D334; -.
DR   STRING; 314608.KT99_16119; -.
DR   Proteomes; UP000005839; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119}.
FT   DOMAIN          8..246
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          384..535
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   582 AA;  64794 MW;  108D3743E7534268 CRC64;
     MPRKYTLKLA HINDTHSHFD ASRIKFCLTH AGKKFDVYSH TGGYARIGHQ INQARIQAKQ
     DKQAFLFLHG GDSFQGTLYF RQFKGVANAH LLNLLKPDAM VLGNHEIDAG NAPVLAFLNN
     IEFPVLAGNM DLSREDASKE SPMSGHPRLL DYDSQTGKAK VLIKQIHDKT LAIIGITLDQ
     MTEIARSDPD IYFINAIETT RKTVAHLKSQ GIDHIIVLSH LGLDQDRLLT DTVDGISLIV
     GGHSHTLQGD FRSLGLSATT YGERVNNTPI LHAGKHAETL GLADIEFDAN GRVTRLQGHN
     YFMLDQQFTL ESAAGVAPED YTAIRSQLEQ HPGILWQQED PQIIRIIASE YRPAIASMDK
     QVLGFLPRDL IHTRLPSKAL PHGSEIAPWV CKGIYHEVKR IHQSVDFALH NAGGVRQSLS
     KGELTLADVI GRLLPFDLPL VKYQILGLYL FETLESAINS ATNNSVTGTG AGSFPYTYGL
     KYCYDGRKPQ GKRILTLEIL CPNSAPEKWI AVDKKQHYVG VSSAYTASGK EGYHPLLKAQ
     WQRPLEELTL ANAFIRFMKR EQTLEQELSP LVSYTSHREA EN
//